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GPVI Protein, Mouse, Recombinant (His)

Catalog No. TMPJ-00605

Glycoprotein VI (GPVI) is a 63 kDa platelet/megakaryocyte-specific type I transmembrane glycoprotein of the immunoglobulin superfamily that is an important collagen receptor and initiator of platelet activation, aggregation and thrombin generation. GPVI is also a secondary receptor required for platelet spreading on laminin. GPVI associates with the Fc receptor gamma -chain via charged aa in the TM domains of GPVI (arginine) and the FcR gamma (aspartic acid). Collagen binding by the GPVI Ig-like domains initiates signaling through the FcR gamma ITAM sequence. Dimerization of GPVI (2:2 with FcR gamma ) and N-glycosylation greatly enhances collagen binding. Type I and III collagens are strong thrombus-forming components in the vascular subendothelium and atherosclerotic plaques. GPVI initiates binding to fibrillar collagens under flow conditions, then activates integrin alpha 2 beta 1 which binds collagen more tightly. GPVI deficiencies cause only a mild bleeding tendency, probably because integrin alpha 2 beta 1 is able to minimally initiate collagen binding. Normal human GPVI concentration can vary widely and affect maximum thrombin generation. Engagement of GPVI by collagens or other agonists, including autoantibodies, causes calmodulin-regulated metalloproteinase cleavage of the 57 kDa ECD and depletes surface GPVI.

GPVI Protein, Mouse, Recombinant (His)

GPVI Protein, Mouse, Recombinant (His)

Catalog No. TMPJ-00605
Glycoprotein VI (GPVI) is a 63 kDa platelet/megakaryocyte-specific type I transmembrane glycoprotein of the immunoglobulin superfamily that is an important collagen receptor and initiator of platelet activation, aggregation and thrombin generation. GPVI is also a secondary receptor required for platelet spreading on laminin. GPVI associates with the Fc receptor gamma -chain via charged aa in the TM domains of GPVI (arginine) and the FcR gamma (aspartic acid). Collagen binding by the GPVI Ig-like domains initiates signaling through the FcR gamma ITAM sequence. Dimerization of GPVI (2:2 with FcR gamma ) and N-glycosylation greatly enhances collagen binding. Type I and III collagens are strong thrombus-forming components in the vascular subendothelium and atherosclerotic plaques. GPVI initiates binding to fibrillar collagens under flow conditions, then activates integrin alpha 2 beta 1 which binds collagen more tightly. GPVI deficiencies cause only a mild bleeding tendency, probably because integrin alpha 2 beta 1 is able to minimally initiate collagen binding. Normal human GPVI concentration can vary widely and affect maximum thrombin generation. Engagement of GPVI by collagens or other agonists, including autoantibodies, causes calmodulin-regulated metalloproteinase cleavage of the 57 kDa ECD and depletes surface GPVI.
Pack SizePriceAvailabilityQuantity
10 μg$1607-10 days
50 μg$4867-10 days
500 μg$2,4407-10 days
1 mg$3,6607-10 days
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Product Information

Biological Activity
Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.
Description
Glycoprotein VI (GPVI) is a 63 kDa platelet/megakaryocyte-specific type I transmembrane glycoprotein of the immunoglobulin superfamily that is an important collagen receptor and initiator of platelet activation, aggregation and thrombin generation. GPVI is also a secondary receptor required for platelet spreading on laminin. GPVI associates with the Fc receptor gamma -chain via charged aa in the TM domains of GPVI (arginine) and the FcR gamma (aspartic acid). Collagen binding by the GPVI Ig-like domains initiates signaling through the FcR gamma ITAM sequence. Dimerization of GPVI (2:2 with FcR gamma ) and N-glycosylation greatly enhances collagen binding. Type I and III collagens are strong thrombus-forming components in the vascular subendothelium and atherosclerotic plaques. GPVI initiates binding to fibrillar collagens under flow conditions, then activates integrin alpha 2 beta 1 which binds collagen more tightly. GPVI deficiencies cause only a mild bleeding tendency, probably because integrin alpha 2 beta 1 is able to minimally initiate collagen binding. Normal human GPVI concentration can vary widely and affect maximum thrombin generation. Engagement of GPVI by collagens or other agonists, including autoantibodies, causes calmodulin-regulated metalloproteinase cleavage of the 57 kDa ECD and depletes surface GPVI.
Species
Mouse
Expression System
HEK293 Cells
TagC-6xHis
Accession NumberB2RR15
Synonyms
platelet glycoprotein VI,MGC138168,GPVIplatelet collagen receptor,GPVI,GPIV,GP6,glycoprotein VI (platelet),Glycoprotein 6
Amino Acid
Gln22-Lys265
Construction
Gln22-Lys265
Protein Purity
Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Molecular Weight40-60 KDa (reducing condition)
Endotoxin< 0.1 ng/µg (1 EU/µg) as determined by LAL test.
FormulationLyophilized from a solution filtered through a 0.22 μm filter, containing PBS, pH 7.4.
Reconstitution
Reconstitute the lyophilized protein in distilled water. The product concentration should not be less than 100 μg/ml. Before opening, centrifuge the tube to collect powder at the bottom. After adding the reconstitution buffer, avoid vortexing or pipetting for mixing.
Stability & Storage
Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
ShippingIn general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice.
Research Background
Glycoprotein VI (GPVI) is a 63 kDa platelet/megakaryocyte-specific type I transmembrane glycoprotein of the immunoglobulin superfamily that is an important collagen receptor and initiator of platelet activation, aggregation and thrombin generation. GPVI is also a secondary receptor required for platelet spreading on laminin. GPVI associates with the Fc receptor gamma -chain via charged aa in the TM domains of GPVI (arginine) and the FcR gamma (aspartic acid). Collagen binding by the GPVI Ig-like domains initiates signaling through the FcR gamma ITAM sequence. Dimerization of GPVI (2:2 with FcR gamma ) and N-glycosylation greatly enhances collagen binding. Type I and III collagens are strong thrombus-forming components in the vascular subendothelium and atherosclerotic plaques. GPVI initiates binding to fibrillar collagens under flow conditions, then activates integrin alpha 2 beta 1 which binds collagen more tightly. GPVI deficiencies cause only a mild bleeding tendency, probably because integrin alpha 2 beta 1 is able to minimally initiate collagen binding. Normal human GPVI concentration can vary widely and affect maximum thrombin generation. Engagement of GPVI by collagens or other agonists, including autoantibodies, causes calmodulin-regulated metalloproteinase cleavage of the 57 kDa ECD and depletes surface GPVI.

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